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LOLA_FRATT
ID   LOLA_FRATT              Reviewed;         205 AA.
AC   Q5NEJ3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Outer-membrane lipoprotein carrier protein {ECO:0000255|HAMAP-Rule:MF_00240};
DE   Flags: Precursor;
GN   Name=lolA {ECO:0000255|HAMAP-Rule:MF_00240}; OrderedLocusNames=FTT_1636;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
CC   -!- FUNCTION: Participates in the translocation of lipoproteins from the
CC       inner membrane to the outer membrane. Only forms a complex with a
CC       lipoprotein if the residue after the N-terminal Cys is not an aspartate
CC       (The Asp acts as a targeting signal to indicate that the lipoprotein
CC       should stay in the inner membrane). {ECO:0000255|HAMAP-Rule:MF_00240}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00240}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00240}.
CC   -!- SIMILARITY: Belongs to the LolA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00240}.
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DR   EMBL; AJ749949; CAG46269.1; -; Genomic_DNA.
DR   RefSeq; WP_003022568.1; NZ_CP010290.1.
DR   RefSeq; YP_170549.1; NC_006570.2.
DR   AlphaFoldDB; Q5NEJ3; -.
DR   SMR; Q5NEJ3; -.
DR   STRING; 177416.FTT_1636; -.
DR   DNASU; 3190782; -.
DR   EnsemblBacteria; CAG46269; CAG46269; FTT_1636.
DR   KEGG; ftu:FTT_1636; -.
DR   eggNOG; COG2834; Bacteria.
DR   OMA; YDPFVEQ; -.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0044874; P:lipoprotein localization to outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042953; P:lipoprotein transport; IEA:InterPro.
DR   CDD; cd16325; LolA; 1.
DR   HAMAP; MF_00240; LolA; 1.
DR   InterPro; IPR029046; LolA/LolB/LppX.
DR   InterPro; IPR004564; OM_lipoprot_carrier_LolA-like.
DR   InterPro; IPR018323; OM_lipoprot_carrier_LolA_Pbac.
DR   PANTHER; PTHR35869; PTHR35869; 1.
DR   Pfam; PF03548; LolA; 1.
DR   SUPFAM; SSF89392; SSF89392; 1.
DR   TIGRFAMs; TIGR00547; lolA; 1.
PE   3: Inferred from homology;
KW   Chaperone; Periplasm; Protein transport; Reference proteome; Signal;
KW   Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00240"
FT   CHAIN           20..205
FT                   /note="Outer-membrane lipoprotein carrier protein"
FT                   /id="PRO_1000071828"
SQ   SEQUENCE   205 AA;  23496 MW;  A5330E72FF3B7F23 CRC64;
     MKKIIICFIF VFSINVSFAD ATSELIDKIK NIHSMTANFN QKLIDGQTNN NLNSKGNMSL
     KKPQYFKWIT TSPNNQEIVS NGTKLWIYDG DLDQLIIKKV SNDIAQFPYL ILLSKNTNNI
     NKLFTVTAQD NNSYILKPKN DQMIDSIKIK FTPNNQLEYL EISTSLNQFT KIEFNNVKTD
     VDISNTSFDF KAPQNTDIID ETKFA
 
 
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